Asian-Australasian Journal of Animal Sciences · 2006 · 45 citations · 32 references
Life SciencesAnimal SciencesBiochemistryCellular MetabolismMetabolismStress PhysiologyHeat StressHeat Stress PhysiologyHeat Stress ToleranceTemperature PhysiologyTemperature ResponsesThermal PhysiologyEnzyme Response To TemperatureEnzymesMalate DehydrogenaseMetabolic Adjustment To Heat StressMetabolic Responses To Heat StressPhysiological Responses To Heat StressTemperature Stress ResponsesThermal Stress Physiology
The metabolic response of Labeo rohita to thermal acclimation was assessed. Advanced fingerlings of L. rohita (average weight 311.4 g) were acclimated to 31, 33 and 36C compared with ambient temperatures (26C) for 30 days and different enzymes associated with stress response were estimated. Glycolytic enzyme-Lactate dehydrogenase, (LDH, E.C.1.1.1.27), TCA cycle enzyme-Malate dehydrogenase (MDH, E.C.1.1.1.37), Protein metabolizing enzymes-Aspartate amino transferase (AST, E.C.2.6.1.1) and Alanine amino transferase (ALT, E.C.2.6.1.2) of liver, gill and muscle, Gluconeogenic enzymes-Fructose 1,6 Bi phosphatase (FBPase, E.C. 3.1.3.11) and Glucose 6 phosphatase (G6Pase, E.C. 3.1.3.9) of liver and kidney were significantly (p<0.05) different with increasing acclimation temperatures. Heat Shock Protein-70 (HSP-70) was expressed in increasing intensity at 31, 33 and 36C but was not expressed at 26C. Results suggest that higher acclimation temperatures enhance metabolism and L. rohita maintains homeostasis between 26-36C via an acclimation episode. Such adaptation appears to be facilitated by resorting to gluconeogenic and glycogenolytic pathways for energy mobilization and induction of HSPs.
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